muramidase and kemptide

muramidase has been researched along with kemptide* in 1 studies

Other Studies

1 other study(ies) available for muramidase and kemptide

Article	Year
Preparing protein microarrays by soft-landing of mass-selected ions. Science (New York, N.Y.), 2003, Sep-05, Volume: 301, Issue:5638 Intact, multiply protonated proteins of particular mass and charge were selected from ionized protein mixtures and gently landed at different positions on a surface to form a microarray. An array of cytochrome c, lysozyme, insulin, and apomyoglobin was generated, and the deposited proteins showed electrospray ionization mass spectra that matched those of the authentic compounds. Deposited lysozyme and trypsin retained their biological activity. Multiply charged ions of protein kinase A catalytic subunit and hexokinase were also soft-landed into glycerol-based liquid surfaces. These soft-landed kinases phosphorylated LRRASLG oligopeptide and D-fructose, respectively. Topics: Apoproteins; Catalytic Domain; Cyclic AMP-Dependent Protein Kinases; Cytochrome c Group; Hexokinase; Insulin; Ions; Mass Spectrometry; Muramidase; Myoglobin; Neurotensin; Oligopeptides; Oligosaccharides; Phosphorylation; Protein Array Analysis; Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin	2003

Article

Year

Preparing protein microarrays by soft-landing of mass-selected ions.

Science (New York, N.Y.), 2003, Sep-05, Volume: 301, Issue:5638

Intact, multiply protonated proteins of particular mass and charge were selected from ionized protein mixtures and gently landed at different positions on a surface to form a microarray. An array of cytochrome c, lysozyme, insulin, and apomyoglobin was generated, and the deposited proteins showed electrospray ionization mass spectra that matched those of the authentic compounds. Deposited lysozyme and trypsin retained their biological activity. Multiply charged ions of protein kinase A catalytic subunit and hexokinase were also soft-landed into glycerol-based liquid surfaces. These soft-landed kinases phosphorylated LRRASLG oligopeptide and D-fructose, respectively.

Topics: Apoproteins; Catalytic Domain; Cyclic AMP-Dependent Protein Kinases; Cytochrome c Group; Hexokinase; Insulin; Ions; Mass Spectrometry; Muramidase; Myoglobin; Neurotensin; Oligopeptides; Oligosaccharides; Phosphorylation; Protein Array Analysis; Proteins; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin

2003